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          Institute: MPI für Biophysik     Collection: Abt. Molekulare Membranbiologie     Display Documents



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ID: 472765.0, MPI für Biophysik / Abt. Molekulare Membranbiologie
Production, characterization and determination of the real catalytic properties of the putative ‘succinate dehydrogenase’ from Wolinella succinogenes
Authors:Juhnke, Hanno D.; Hiltscher, Heiko; Nasiri, Hamid R.; Schwalbe, Harald; Lancaster, C. Roy D.
Language:English
Date of Publication (YYYY-MM-DD):2009
Title of Journal:Molecular Microbiology
Journal Abbrev.:Mol. Microbiol.
Volume:71
Issue / Number:5
Start Page:1088
End Page:1101
Review Status:Peer-review
Audience:Experts Only
Abstract / Description:Both the genomes of the epsilonproteobacteria Wolinella succinogenes and Campylobacter jejuni contain operons (sdhABE) that encode for so far uncharacterized enzyme complexes annotated as ‘non-classical’ succinate:quinone reductases (SQRs). However, the role of such an enzyme ostensibly involved in aerobic respiration in an anaerobic organism such as W. succinogenes has hitherto been unknown. We have established the first genetic system for the manipulation and production of a member of the non-classical succinate:quinone oxidoreductase family. Biochemical characterization of the W. succinogenes enzyme reveals that the putative SQR is in fact a novel methylmenaquinol:fumarate reductase (MFR) with no detectable succinate oxidation activity, clearly indicative of its involvement in anaerobic metabolism. We demonstrate that the hydrophilic subunits of the MFR complex are, in contrast to all other previously characterized members of the superfamily, exported into the periplasm via the twin-arginine translocation (tat)-pathway. Furthermore we show that a single amino acid exchange (Ala86,His) in the flavoprotein of that enzyme complex is the only additional requirement for the covalent binding of the otherwise non-covalently bound FAD. Our results provide an explanation for the previously published puzzling observation that the C. jejuni sdhABE operon is upregulated in an oxygenlimited environment as compared with microaerophilic laboratory conditions
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für Biophysik/Abteilung Molekulare Membranbiologie
External Affiliations:Cluster of Excellence ‘Macromolecular Complexes’, Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, Max-von-Laue-Str. 3, D-60438 Frankfurt am Main, Germany;
Cluster of Excellence ‘Macromolecular Complexes’, Institute of Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Johann Wolfgang Goethe University, Max-von-Laue-Str. 7, D-60438 Frankfurt am Main, Germany;
Department of Structural Biology, Faculty of Medicine, Saarland University, D-66421 Homburg (Saar), Germany
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